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Updated: Jul 24, 2026

Real-time Analyses of Retinol Transport by the Membrane Receptor of Plasma Retinol Binding Protein
Published on: January 28, 2013
Cellular retinoic acid binding protein is associated with mitochondria
1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Abstract:
We report that immunohistochemical staining for cellular retinoic acid-binding protein (CRABP) was restricted to the cytoplasm of cortical cells in bovine adrenal. In contrast, staining for the similar protein, cellular retinol-binding protein (CRBP), was found throughout these cells. After transfections of CRABP and CRBP into cultured cells, immunofluorescence analyses again revealed cytoplasmic restriction only for CRABP, with a pronounced punctate appearance. Use of organelle-specific fluorochromes indicated that CRABP immunofluorescence overlaid exactly with the pattern of the mitochondrial-specific fluorochrome. Confirmation of this association came with subcellular fractionation of the adrenal cortex. CRABP, but not CRBP, co-sedimented with the mitochondria, a novel finding for a member of this superfamily of cellular lipid-binding proteins.
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